Authors: Niccolai N, Ciutti A, Spiga O, Scarselli M, Bernini A, Bracci L, Di Maro D, Dalvit C, Molinari H, Esposito G, Temussi PA
Characterization of protein surface accessibility represents a new frontier of structural biology. A surface accessibility investigation for two structurally well-defined proteins, tendamistat and bovine pancreatic trypsin inhibitor, is performed here by a combined analysis of water-protein Overhauser effects and paramagnetic perturbation profiles induced by the soluble spin-label 4-hydroxy-2,2,6,6-tetramethyl-piperidine-1-oxyl on NMR spectra. This approach seems to be reliable not only for distinguishing between buried and exposed residues but also for finding molecular locations where a network of more ordered waters covers the protein surface. From the presented set of data, an overall picture of the surface accessibility of the two proteins can be inferred. Detailed knowledge of protein accessibility can form the basis for successful design of mutants with increased activity and/or greater specificity.
NMR characterizations of the ice binding surface of an antifreeze protein.
NMR characterizations of the ice binding surface of an antifreeze protein.
NMR characterizations of the ice binding surface of an antifreeze protein.
PLoS One. 2010;5(12):e15682
Authors: Hong J, Hu Y, Li C, Jia Z, Xia B, Jin C
Antifreeze protein (AFP) has a unique function of reducing solution freezing temperature to protect organisms from ice damage. However, its functional mechanism is not well understood. An intriguing question concerning AFP function is how the high selectivity for ice ligand is achieved in the presence of free water of...
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[NMR paper] Paramagnetic NMR study of Cu(2+)-IDA complex localization on a protein surface and it
Paramagnetic NMR study of Cu(2+)-IDA complex localization on a protein surface and its application to elucidate long distance information.
Related Articles Paramagnetic NMR study of Cu(2+)-IDA complex localization on a protein surface and its application to elucidate long distance information.
FEBS Lett. 2004 May 21;566(1-3):157-61
Authors: Nomura M, Kobayashi T, Kohno T, Fujiwara K, Tenno T, Shirakawa M, Ishizaki I, Yamamoto K, Matsuyama T, Mishima M, Kojima C
The paramagnetic metal chelate complex Cu(2+)-iminodiacetic acid (Cu(2+)-IDA) was...
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11-24-2010 09:51 PM
[NMR paper] NMR studies of protein hydration and TEMPOL accessibility.
NMR studies of protein hydration and TEMPOL accessibility.
Related Articles NMR studies of protein hydration and TEMPOL accessibility.
J Mol Biol. 2003 Sep 12;332(2):437-47
Authors: Niccolai N, Spiga O, Bernini A, Scarselli M, Ciutti A, Fiaschi I, Chiellini S, Molinari H, Temussi PA
Understanding the mechanisms of the interaction between a protein surface and its outer molecular environment is of primary relevance for the rational design of new drugs and engineered proteins. Protein surface accessibility is emerging as a new dimension of...
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11-24-2010 09:16 PM
[NMR paper] Probing the surface of a sweet protein: NMR study of MNEI with a paramagnetic probe.
Probing the surface of a sweet protein: NMR study of MNEI with a paramagnetic probe.
Related Articles Probing the surface of a sweet protein: NMR study of MNEI with a paramagnetic probe.
Protein Sci. 2001 Aug;10(8):1498-507
Authors: Niccolai N, Spadaccini R, Scarselli M, Bernini A, Crescenzi O, Spiga O, Ciutti A, Di Maro D, Bracci L, Dalvit C, Temussi PA
The design of safe sweeteners is very important for people who are affected by diabetes, hyperlipemia, and caries and other diseases that are linked to the consumption of sugars. Sweet...
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11-19-2010 08:44 PM
[NMR paper] Novel mechanism of surface catalysis of protein adduct formation. NMR studies of the
Novel mechanism of surface catalysis of protein adduct formation. NMR studies of the acetylation of ubiquitin.
Related Articles Novel mechanism of surface catalysis of protein adduct formation. NMR studies of the acetylation of ubiquitin.
J Biol Chem. 2000 Oct 13;275(41):31908-13
Authors: Macdonald JM, Haas AL, London RE
Reactivity of surface lysyl residues of proteins with a broad range of chemical agents has been proposed to be dependent on the catalytic microenvironment of the residue. We have investigated the acetylation of wild type...
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11-19-2010 08:29 PM
[NMR paper] Identification of the DNA binding surface of H-NS protein from Escherichia coli by he
Identification of the DNA binding surface of H-NS protein from Escherichia coli by heteronuclear NMR spectroscopy.
Related Articles Identification of the DNA binding surface of H-NS protein from Escherichia coli by heteronuclear NMR spectroscopy.
FEBS Lett. 1999 Jul 16;455(1-2):63-9
Authors: Shindo H, Ohnuki A, Ginba H, Katoh E, Ueguchi C, Mizuno T, Yamazaki T
The DNA binding domain of H-NS protein was studied with various N-terminal deletion mutant proteins and identified by gel retardation assay and heteronuclear 2D- and 3D-NMR...
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[NMR paper] Probing protein structure by solvent perturbation of NMR spectra: the surface accessi
Probing protein structure by solvent perturbation of NMR spectra: the surface accessibility of bovine pancreatic trypsin inhibitor.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Probing protein structure by solvent perturbation of NMR spectra: the surface accessibility of bovine pancreatic trypsin inhibitor.
Biophys J. 1997 Jul;73(1):382-96
Authors: Molinari H,...
NMR studies of protein surface accessibility.
Linear Mode
